3FCK

Complex of UNG2 and a fragment-based design inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0004844	molecular_function	uracil DNA N-glycosylase activity
B	0006281	biological_process	DNA repair
B	0006284	biological_process	base-excision repair
B	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE FCK B 1

Functional Information from PROSITE/UniProt

site_id	PS00130
Number of Residues	10
Details	U_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVVIlGQDPY

Chain	Residue	Details
B	LYS138-TYR147

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03166","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9724657","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SSP","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8900285","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9724657","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SSP","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4SKN","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8900285","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4SKN","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1eug